| Literature DB >> 6825861 |
J A Biosca, F Travers, T E Barman.
Abstract
The temperature dependence of the kinetics of the binding of ATP to myosin subfragment-1 was studied by an ATP chase technique in a rapid-flow-quench apparatus: (formula; see text) A temperature range of 30 degrees C to -15 degrees C was obtained with ethylene glycol as antifreeze. The Arrhenius plot of k2 is discontinuous with a jump at 12 degrees C. Above the jump delta H+ = 9.5 kcal/mol, below delta H+ = 28.5 kcal/mol. Few such Arrhenius plots are recorded in the literature but they are predicted from theory. Thus, we explain our results as a phase change of the subfragment 1-ATP system at 12 degrees C. This is in agreement with certain structural studies.Entities:
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Year: 1983 PMID: 6825861 DOI: 10.1016/0014-5793(83)80151-3
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124